B.S in Chemistry, Lehman College, City University of New York, NY, 1996.
Ph.D. in Chemistry, State University of New York at Stony Brook, 2001.
Contemporary Chemistry (CHEM 055) This is an introductory chemistry course for students who either have a limited background or no background in chemistry. (Fall 2009).
Survey of Chemistry (CHEM 103) This course is designed to provide health science and liberal arts students with a general overview of basic chemical concepts. (Fall 2008).
General Chemistry (CHEM 105 - 106) This course covers all the basic concepts of chemistry. The concepts at this level can be reinforced nicely through use of examples which relate chemistry to environmental, health and industrial problems. (Spring 2013).
Physical Chemistry and Laboratory (Chem 331, 332, 333L) The first semester provides a quantitative study of the principles of thermodynamics, kinetic molecular theory of gases, and chemical kinetics. Applications to solutions, phase equilibria, chemical reactions and transport properties are explored. A brief introduction to quantum mechanics and spectroscopy is made. The second semester covers principles of quantum mechanics with application to atomic and molecular structure and spectroscopy. It also provides an introduction to statistical mechanics. (Spring 2011).
Dynamics and folding of proteins using solution and solid-state nuclear magnetic resonance techniques and theoretical/computational approaches.
One of the proteins I look at is a classic model system of protein folding studies: chicken villin headpiece subdomain (HP35). It is a small protein consisting of 35 amino acids which span three helices. The ribbon diagram is shown in the figure below.
Three-dimensional molecular shapes of proteins have been long recognized to play an important role in their biological functions. Many structural studies have been performed that aim at finding exact structures of proteins. In the past decade it became clear that protein molecules “breathe” and their structures fluctuate.
It turned out that this breathing has important consequences for specific functions and characteristics of proteins.
My studies investigate the dynamics of proteins on various time scales and at various conditions: in solution and solids phases, at temperatures from 4K to 300K by experimental and computational approaches.
Nuclear Magnetic Resonance (NMR) techniques are particularly suitable for the investigation of protein dynamics, since they allow measurements at many sites on a protein molecule, thus providing us with the picture of what’s going on in various parts of the protein. Further, these techniques can be sensitive to motions
over a very broad range of time scales, from picoseconds (10-9sec) to seconds. I use NMR as a major experimental tool to probe protein dynamics. In addition, I use a number of theoretical and computation approaches for data analysis and interpretation.
- Vugmeyster L, Ostrovsky D, Penland K, Ellden J, Hoatson GL, Vold RL, accepted to J. Phys. Chem.B. http://dx.doi.org/10.1021/jp311112j, (2013)"Glassy Dynamics of Protein Methyl Groups Revealed by Deuteron NMR"
- Vugmeyster L, Do T, Ostrovsky D, Fu R, Hagedorn B. Solid State NMR, 45-46, 11-15 (2012) “Characterization of Water Dynamics in Frozen Soils by Solid-State Deuteron NMR”
- Vugmeyster L, Ostrovsky D, Khadjinova A, Ellden J, Hoatson GL, Vold RL, Biochemistry, 50, 10637–10646(2011) “Slow Motions in The Hydrophobic Core of Chicken Villin Headpiece Subdomain and their Contributions to Configurational Entropy and Heat Capacity from Solid-State Deuteron NMR measurements”
- Vugmeyster L, Ostrovsky D, J. Biomol. NMR, 50(2), 119-127 (2011) “Temperature Dependence of Fast Carbonyl Backbone Dynamics in Chicken Villin Headpiece Subdomain”
- Vugmeyster L, Ostrovsky D, Li, Y, J. Biomol. NMR 47 (2), 155-162 (2010) "Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites In dematin headpiece C-terminal domain and Its S74E mutant."
- Vugmeyster L, Ostrovsky D, Ford JJ, Lipton AS, J. Am. Chem. Soc. 132 (12), 4038–4039 (2010) "Freezing of dynamics of a methyl group in a protein hydrophobic core at cryogenic temperatures by deuteron NMR spectroscopy."
- Vugmeyster L, Ostrovsky D, Ford JJ, Burton SD, Lipton AS, Hoatson GL, Vold RL, J. Am. Chem. Soc. 131 (38), 13651–13658 (2009) "Probing the dynamics of a protein hydrophobic core by deuteron solid-state nuclear magnetic resonance spectroscopy."
- Vold RL, Hoatson GL, Vugmeyster L, Ostrovsky D, DeCasto PJ, Phys. Chem. Chem. Phys. 11, 7008-7012 (2009) "Solid State Deuteron Relaxation Time Anisotropy Measured With Multiple Echo Acquisition."
- Vugmeyster L Magn. Reson. Chem. 47, 746-751 (2009) "Slow Backbone Dynamics of Chicken Villin Headpiece Subdomain Probed by NMR C′-N Cross-Correlated Relaxation."
- Vugmeyster L, Ostrovsky D, Ford JJ, Burton SD, Lipton AS, Hoatson GL, Vold RL, accepted to J. Am. Chem. Soc. ASAP (web) DOI: 10.1021/ja902977u (2009) "Probing the Dynamics of a Protein Hydrophobic Core by Deuteron Solid-State Nuclear Magnetic Resonance Spectroscopy."
- Vugmeyster L, McKnight CJ, J Biomol NMR 43, 39-50 (2009) "Phosphorylation-induced changes in backbone dynamics of dematin headpiece C-terminal subdomain."
- Vugmeyster L, McKnight CJ, Biophys J 95, 5941-5960 (2008) "Slow Motions in Chicken Villin Headpiece Subdomain Probed by Cross-correlated NMR Relaxation of Amide NH Bonds in Successive Residues."
- Vugmeyster L, Bodenhausen G, Appl Magn Reson 28, 147-163 (2005) "Temperature dependent protein backbone dynamics from auto- and cross-correlated NMR relaxation rates."
- Vugmeyster L, Perazzolo C, Wist J, Frueh D, Bodenhausen G, J Biomol NMR 28, (2), 173-177 (2004) "Evidence of slow motions by cross-correlated chemical shift modulation in deuterated and protonated proteins."
- Vugmeyster L, Pelupessy P, Vugmeister BE, Abergel D, Bodenhausen G, Comptes Rendus de l'Académie des Sciences (section de Physique) 5 (3), 377-386 (2004) "Cross-correlated relaxation in NMR of macromolecules in the presence of fast and slow dynamics."
- Wang M, Tang Y, Sato S, Vugmeyster L, McKnight CJ, Raleigh DP, J Am Chem Soc 125 (20), 6032-6033 (2003) "Dynamic NMR lineshape analysis demonstrates that the Villin Headpiece Domain folds on the microsecond time scale."
- Vugmeyster L, Raleigh DP, Palmer AG, Vugmeister BE, J Am Chem Soc 125 (27), 8400-8404 (2003) "Beyond the decoupling approximation in the model free approach for the interpretation of NMR relaxation of macromolecules in solution."
- Vugmeyster L, Trott O, McKnight CJ, Raleigh DP, Palmer AG, J Mol Biol, 320 (4), 841-854 (2002) "Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein."
- Vugmeyster L, Kroenke CD, Picart F, Palmer AG, Raleigh DP, J Am Chem Soc , 122 (22), 5387-5388 (2000) "N15 R1rho measurements allow the determination of ultrafast protein folding rates."
- Vugmeyster L, Kuhlman B, Raleigh DP, Protein Science, 7 (9), 1994-1997 (1998) "Amide proton exchange measurements as a probe of the stability and dynamics of the N-terminal domain of the ribosomal protein L9: Comparison with the intact protein."